ID   ARCA_STRPG              Reviewed;         411 AA.
AC   P58827; A2RDI9;
DT   27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   17-APR-2007, sequence version 3.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Arginine deiminase;
DE            Short=ADI;
DE            EC=3.5.3.6;
DE   AltName: Full=Arginine dihydrolase;
DE            Short=AD;
DE   AltName: Full=Streptococcal acid glycoprotein;
GN   Name=arcA; Synonyms=sagP; OrderedLocusNames=SpyM50577;
OS   Streptococcus pyogenes serotype M5 (strain Manfredo).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=160491;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Manfredo;
RX   PubMed=17012393; DOI=10.1128/jb.01227-06;
RA   Holden M.T.G., Scott A., Cherevach I., Chillingworth T., Churcher C.,
RA   Cronin A., Dowd L., Feltwell T., Hamlin N., Holroyd S., Jagels K.,
RA   Moule S., Mungall K., Quail M.A., Price C., Rabbinowitsch E., Sharp S.,
RA   Skelton J., Whitehead S., Barrell B.G., Kehoe M., Parkhill J.;
RT   "Complete genome of acute rheumatic fever-associated serotype M5
RT   Streptococcus pyogenes strain Manfredo.";
RL   J. Bacteriol. 189:1473-1477(2007).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-16, AND CHARACTERIZATION.
RX   PubMed=9632565; DOI=10.1128/iai.66.7.3050-3058.1998;
RA   Degnan B.A., Palmer J.M., Robson T., Jones C.E.D., Fischer M.,
RA   Glanville M., Mellor G.D., Diamond A.G., Kehoe M.A., Goodacre J.A.;
RT   "Inhibition of human peripheral blood mononuclear cell proliferation by
RT   Streptococcus pyogenes cell extract is associated with arginine deiminase
RT   activity.";
RL   Infect. Immun. 66:3050-3058(1998).
CC   -!- FUNCTION: Antitumor protein. Has a powerful and dose-dependent
CC       inhibitory effect on antigen, superantigen, or mitogen-stimulated human
CC       peripheral blood mononuclear cell (PBMC) proliferation. It may inhibit
CC       cell proliferation by arresting cell cycle and inducing apoptosis.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-arginine = L-citrulline + NH4(+);
CC         Xref=Rhea:RHEA:19597, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:32682, ChEBI:CHEBI:57743; EC=3.5.3.6;
CC   -!- PATHWAY: Amino-acid degradation; L-arginine degradation via ADI
CC       pathway; carbamoyl phosphate from L-arginine: step 1/2.
CC   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- PTM: Glycosylated. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the arginine deiminase family. {ECO:0000305}.
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DR   EMBL; AM295007; CAM29914.1; -; Genomic_DNA.
DR   RefSeq; WP_011888729.1; NC_009332.1.
DR   AlphaFoldDB; P58827; -.
DR   SMR; P58827; -.
DR   PRIDE; P58827; -.
DR   KEGG; spf:SpyM50577; -.
DR   HOGENOM; CLU_052662_0_1_9; -.
DR   OMA; ERATMHL; -.
DR   UniPathway; UPA00254; UER00364.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016990; F:arginine deiminase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0019547; P:arginine catabolic process to ornithine; IEA:UniProtKB-UniPathway.
DR   GO; GO:0018101; P:protein citrullination; IEA:GOC.
DR   HAMAP; MF_00242; Arg_deiminase; 1.
DR   InterPro; IPR003876; Arg_deiminase.
DR   PIRSF; PIRSF006356; Arg_deiminase; 1.
DR   PRINTS; PR01466; ARGDEIMINASE.
DR   TIGRFAMs; TIGR01078; arcA; 1.
PE   1: Evidence at protein level;
KW   Arginine metabolism; Cytoplasm; Direct protein sequencing; Glycoprotein;
KW   Hydrolase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:9632565"
FT   CHAIN           2..411
FT                   /note="Arginine deiminase"
FT                   /id="PRO_0000182250"
FT   ACT_SITE        401
FT                   /note="Amidino-cysteine intermediate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   411 AA;  46311 MW;  7011E3E1A03649C0 CRC64;
     MTAQTPIHVY SEIGKLKKVL LHRPGKEIEN LMPDYLERLL FDDIPFLEDA QKEHDAFAQA
     LRDEGIEVLY LETLAAESLV TPEIREAFID EYLSEANIRG RATKKAIREL LMAIEDNQEL
     IEKTMAGVQK SELPEIPASE KGLTDLVESN YPFAIDPMPN LYFTRDPFAT IGTGVSLNHM
     FSETRNRETL YGKYIFTHHP IYGGGKVPMV YDRNETTRIE GGDELVLSKD VLAVGISQRT
     DAASIEKLLV NIFKQNLGFK KVLAFEFANN RKFMHLDTVF TMVDYDKFTI HPEIEGDLRV
     YSVTYDNEEL HIIEEKGDLA ELLAANLGVE KVDLIRCGGD NLVAAGREQW NDGSNTLTIA
     PGVVVVYNRN TITNAILESK GLKLIKIHGS ELVRGRGGPR CMSMPFERED I